Quantitation of pathways of ethanol metabolism
Autor: | Howard B. Feldman, Roger J.M. Corrall, Joseph M. Margolis, Ling C. Yu, Ming S. Kong, Patricia A. Szczepanik, Peter J. Klein, Marc A. Abrams, Bernard R. Landau, Pamela Havre |
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Rok vydání: | 1977 |
Předmět: |
Biophysics
Biochemistry chemistry.chemical_compound Stereospecificity Species Specificity Animals Sorbitol Ethanol metabolism Molecular Biology Alcohol dehydrogenase Ethanol biology Liver cell Metabolism Aldehyde Oxidoreductases Rats Alcohol Oxidoreductases Glucose Liver chemistry Catalase Microsomes Liver biology.protein Cattle Female |
Zdroj: | Archives of Biochemistry and Biophysics. 182:14-23 |
ISSN: | 0003-9861 |
DOI: | 10.1016/0003-9861(77)90278-8 |
Popis: | A method has been developed for estimating the sum of the contributions to ethanol oxidation by the microsomal ethanol-oxidizing system (MEOS) and catalase in the intact liver cell. It depends upon a comparison of the fate of the R hydrogen of ethanol and the hydrogen bound to carbon-2 of sorbitol under identical conditions. Limitations of the approach, particularly as regards isotopic effects, are defined. Under the condition of incubation of liver slices from rat and monkey at a concentration of ethanol of 3 mg/ml and from rat at 1 mg/ml, alcohol dehydrogenase catalysis is concluded to account, on the average, for 89% or more of the initial metabolism of ethanol. As by-products of this study, the stereospecificity of the sorbitol dehydrogenase-catalyzed reaction is shown to be of the A type in the rat, and evidence is obtained for the irreversibility of sorbitol oxidation in the intact liver cell. |
Databáze: | OpenAIRE |
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